3DPB
Crystal structure of the complex of the Caf1M chaperone with the mini-fiber of two Caf1 subunits (Caf1:Caf1), carrying the Ala9Val, Ala11Val, and Leu13Val mutations in the Gd donor strand
Summary for 3DPB
Entry DOI | 10.2210/pdb3dpb/pdb |
Related | 1P5U 1Z9S 3DOS 3DSN |
Descriptor | Chaperone protein caf1M, F1 capsule antigen (3 entities in total) |
Functional Keywords | donor strand complementation, fimbriae, chaperone, protein-protein complex, beta barrel, immunoglobulin domain, periplasm, plasmid, capsule, secreted, chaperone-structural protein complex, chaperone/structural protein |
Biological source | Yersinia pestis More |
Cellular location | Periplasm: P26926 Secreted, capsule: P26948 |
Total number of polymer chains | 3 |
Total formula weight | 57563.48 |
Authors | Fooks, L.J.,Yu, X.,Moslehi-Mohebi, E.,Tischenko, V.,Knight, S.D.,MacIntyre, S.,Zavialov, A.V. (deposition date: 2008-07-07, release date: 2009-07-14, Last modification date: 2023-08-30) |
Primary citation | Fooks, L.J.,Yu, X.,Moslehi-Mohebi, E.,Tischenko, V.,Knight, S.D.,MacIntyre, S.,Zavialov, A.V. Hydrophobicity and rigidity of binding segments enable CAF1M chaperone to act as assembly catalyst To be published, |
Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
Download full validation report